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Volumn 13, Issue 10, 2002, Pages 3546-3559

Fibronectin polymerization regulates the composition and stability of extracellular matrix fibrils and cell-matrix adhesions

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; FIBRONECTIN; INTEGRIN; THROMBOSPONDIN 1; ACTIN; ANTINEOPLASTIC AGENT; CYCLOPEPTIDE; DEPSIPEPTIDE; JASPAMIDE; MITOGEN ACTIVATED PROTEIN KINASE; PEPTIDE FRAGMENT; POLYMER; PROTEINASE INHIBITOR; RADIOACTIVE IODINE;

EID: 0036796746     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E02-01-0048     Document Type: Article
Times cited : (495)

References (89)
  • 1
    • 0024359871 scopus 로고
    • Analysis of fibronectin receptor function with monoclonal antibodies: Roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization
    • Akiyama, S.K., Yamada, S.S., Chen, W.T., and Yamada, K.M. (1989). Analysis of fibronectin receptor function with monoclonal antibodies: roles in cell adhesion, migration, matrix assembly, and cytoskeletal organization. J. Cell Biol. 109, 863-875.
    • (1989) J. Cell Biol. , vol.109 , pp. 863-875
    • Akiyama, S.K.1    Yamada, S.S.2    Chen, W.T.3    Yamada, K.M.4
  • 2
    • 0023791465 scopus 로고
    • Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts
    • Allen-Hoffmann, B.L., Crankshaw, C.L., and Mosher, D.F. (1988). Transforming growth factor beta increases cell surface binding and assembly of exogenous (plasma) fibronectin by normal human fibroblasts. Mol. Cell. Biol. 8, 4234-4242.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4234-4242
    • Allen-Hoffmann, B.L.1    Crankshaw, C.L.2    Mosher, D.F.3
  • 3
    • 0032514841 scopus 로고    scopus 로고
    • Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all αv integrins
    • Bader, B.L., Rayburn, H., Crowley, D., and Hynes, R.O. (1998). Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all αv integrins. Cell 95, 507-519.
    • (1998) Cell , vol.95 , pp. 507-519
    • Bader, B.L.1    Rayburn, H.2    Crowley, D.3    Hynes, R.O.4
  • 4
    • 0023805668 scopus 로고
    • Factor XIII cross-klinking of fibronectin at cellular matrix assembly sites
    • Barry, E.L.R., and Mosher, D.F. (1988). Factor XIII cross-klinking of fibronectin at cellular matrix assembly sites. J. Biol. Chem. 263, 10464-10469.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10464-10469
    • Barry, E.L.R.1    Mosher, D.F.2
  • 6
    • 0032487438 scopus 로고    scopus 로고
    • Fibronectin matrix regulates activation of RHO and CDC42 GTPases and cell cycle progression
    • Bourdoulous, S., Orend, G., MacKenna, D.A., Pasqualini, R., and Ruoslahti, E. (1998). Fibronectin matrix regulates activation of RHO and CDC42 GTPases and cell cycle progression. J. Cell Biol. 143, 267-276.
    • (1998) J. Cell Biol. , vol.143 , pp. 267-276
    • Bourdoulous, S.1    Orend, G.2    MacKenna, D.A.3    Pasqualini, R.4    Ruoslahti, E.5
  • 7
    • 0028244823 scopus 로고
    • Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin
    • Bubb, M.R., Senderowicz, A.M., Sausville, E.A., Duncan, K.L., and Korn, E.D. (1994). Jasplakinolide, a cytotoxic natural product, induces actin polymerization and competitively inhibits the binding of phalloidin to F-actin. J. Biol. Chem. 269, 14869-14871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14869-14871
    • Bubb, M.R.1    Senderowicz, A.M.2    Sausville, E.A.3    Duncan, K.L.4    Korn, E.D.5
  • 8
    • 0034681423 scopus 로고    scopus 로고
    • Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations
    • Bubb, M.R., Spector, I., Beyer, B.B., and Fosen, K.M. (2000). Effects of jasplakinolide on the kinetics of actin polymerization. An explanation for certain in vivo observations. J. Biol. Chem. 275, 5163-5170.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5163-5170
    • Bubb, M.R.1    Spector, I.2    Beyer, B.B.3    Fosen, K.M.4
  • 9
    • 0020411692 scopus 로고
    • Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts
    • Chen, W.T., and Singer, S.J. (1982). Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts. J. Cell Biol. 95, 205-222.
    • (1982) J. Cell Biol. , vol.95 , pp. 205-222
    • Chen, W.T.1    Singer, S.J.2
  • 10
    • 0025730907 scopus 로고
    • Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular matrix
    • Chernousov, M.A., Fogerty, F.J., Koteliansky, V.E., and Mosher, D.F. (1991). Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular matrix. J. Biol. Chem. 266, 10851-10858.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10851-10858
    • Chernousov, M.A.1    Fogerty, F.J.2    Koteliansky, V.E.3    Mosher, D.F.4
  • 11
    • 0018583163 scopus 로고
    • Biosynthesis and processing of fibronectin in NIL.8 hamster cells
    • Choi, M.G., and Hynes, R.O. (1979). Biosynthesis and processing of fibronectin in NIL.8 hamster cells. J. Biol. Chem. 23, 12050-12055.
    • (1979) J. Biol. Chem. , vol.23 , pp. 12050-12055
    • Choi, M.G.1    Hynes, R.O.2
  • 12
    • 0030839023 scopus 로고    scopus 로고
    • Glycosaminoglycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C
    • Chung, C.Y., and Erickson, H.P. (1997). Glycosaminoglycans modulate fibronectin matrix assembly and are essential for matrix incorporation of tenascin-C. J. Cell Sci. 110, 1413-1419.
    • (1997) J. Cell Sci. , vol.110 , pp. 1413-1419
    • Chung, C.Y.1    Erickson, H.P.2
  • 13
    • 0028866433 scopus 로고
    • Binding of tenascin-C to soluble fibronectin and matrix fibrils
    • Chung, C.Y., Zardi, L., and Erickson, H.P. (1995). Binding of tenascin-C to soluble fibronectin and matrix fibrils. J. Biol. Chem. 270, 29012-29017.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29012-29017
    • Chung, C.Y.1    Zardi, L.2    Erickson, H.P.3
  • 14
    • 0031013741 scopus 로고    scopus 로고
    • TGF-β1 stimulates cultured human fibroblasts to proliferate and produce tissue-like fibroplasia: A fibronectin matrix-dependent event
    • Clark, R.A.F., McCoy, G.A., Folkvord, J.M., and McPherson, J.M. (1997). TGF-β1 stimulates cultured human fibroblasts to proliferate and produce tissue-like fibroplasia: a fibronectin matrix-dependent event. J. Cell. Physiol. 170, 69-80.
    • (1997) J. Cell. Physiol. , vol.170 , pp. 69-80
    • Clark, R.A.F.1    McCoy, G.A.2    Folkvord, J.M.3    McPherson, J.M.4
  • 15
    • 0033006918 scopus 로고    scopus 로고
    • Elastin: Molecular description and function
    • Debelle, L., and Tamburro, A.M. (1999). Elastin: molecular description and function. Int. J. Biochem. Cell Biol. 31, 261-272.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 261-272
    • Debelle, L.1    Tamburro, A.M.2
  • 16
    • 0033932709 scopus 로고    scopus 로고
    • Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction
    • Ducharme, A. et al. (2000). Targeted deletion of matrix metalloproteinase-9 attenuates left ventricular enlargement and collagen accumulation after experimental myocardial infarction. J. Clin. Invest. 106, 55-62.
    • (2000) J. Clin. Invest. , vol.106 , pp. 55-62
    • Ducharme, A.1
  • 18
    • 0030818072 scopus 로고    scopus 로고
    • Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells
    • George, E.L., Baldwin, H.S., and Hynes, R.O. (1997). Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells. Blood 90, 3073-3081.
    • (1997) Blood , vol.90 , pp. 3073-3081
    • George, E.L.1    Baldwin, H.S.2    Hynes, R.O.3
  • 19
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George, E.L., Georges-Labousse, E.N., Patel-King, R.S., Rayburn, H., and Hynes, R.O. (1993). Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119, 1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labousse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 21
    • 0029007213 scopus 로고
    • Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1
    • Godyna, S., Liau, G., Popa, I., Stefansson, S., and Argraves, W.S. (1995a). Identification of the low density lipoprotein receptor-related protein (LRP) as an endocytic receptor for thrombospondin-1. J. Cell Biol. 129, 1403-1410.
    • (1995) J. Cell Biol. , vol.129 , pp. 1403-1410
    • Godyna, S.1    Liau, G.2    Popa, I.3    Stefansson, S.4    Argraves, W.S.5
  • 22
    • 0028648870 scopus 로고
    • A quantitative analysis of the incorporation of fibulin-1 into extracellular matrix indicates that fibronectin assembly is required
    • Godyna, S., Mann, D.M., and Argraves, W.S. (1995b). A quantitative analysis of the incorporation of fibulin-1 into extracellular matrix indicates that fibronectin assembly is required. Matrix Biol. 14, 467-477.
    • (1995) Matrix Biol. , vol.14 , pp. 467-477
    • Godyna, S.1    Mann, D.M.2    Argraves, W.S.3
  • 23
    • 0025147371 scopus 로고
    • A tumor suppressor-dependant inhibitor of angiogenesis is immunologically and fuctionally indistinguishable from a fragment of thrombospondin
    • Good, D.J., Polverini, P.J., Rastinejad, F., LeBeau, M.M., Lemons, R.S., Frazier, W.A., and Bouck, N.P. (1990). A tumor suppressor-dependant inhibitor of angiogenesis is immunologically and fuctionally indistinguishable from a fragment of thrombospondin. Proc. Natl. Acad. Sci. USA 87, 6624-6628.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6624-6628
    • Good, D.J.1    Polverini, P.J.2    Rastinejad, F.3    LeBeau, M.M.4    Lemons, R.S.5    Frazier, W.A.6    Bouck, N.P.7
  • 24
    • 0034715896 scopus 로고    scopus 로고
    • Insights into extracellular matrix functions from mutant mouse models
    • Gustafsson, E., and Fassler, R. (2000). Insights into extracellular matrix functions from mutant mouse models. Exp. Cell Res. 261, 52-68.
    • (2000) Exp. Cell Res. , vol.261 , pp. 52-68
    • Gustafsson, E.1    Fassler, R.2
  • 25
    • 0026764872 scopus 로고
    • Endocytosis of different members of the small chondroitin/dermatan sulfate proteoglycan family
    • Hausser, H., Ober, B., Quentin-Hoffmann, E., Schmidt, B., and Kresse, H. (1992). Endocytosis of different members of the small chondroitin/dermatan sulfate proteoglycan family. J. Biol. Chem. 267, 11559-11564.
    • (1992) J. Biol. Chem. , vol.267 , pp. 11559-11564
    • Hausser, H.1    Ober, B.2    Quentin-Hoffmann, E.3    Schmidt, B.4    Kresse, H.5
  • 26
    • 0029897753 scopus 로고    scopus 로고
    • A novel role for the integrin-binding III-10 module in fibronectin matrix assembly
    • Hocking, D.C., Smith, R.K., and McKeown-Longo, P.J. (1996). A novel role for the integrin-binding III-10 module in fibronectin matrix assembly. J. Cell Biol. 133, 431-444.
    • (1996) J. Cell Biol. , vol.133 , pp. 431-444
    • Hocking, D.C.1    Smith, R.K.2    McKeown-Longo, P.J.3
  • 27
    • 0034616386 scopus 로고    scopus 로고
    • Stimulation of integrin-mediated cell contractility by fibronectin polymerization
    • Hocking, D.C., Sottile, J., and Langenbach, K.J. (2000). Stimulation of integrin-mediated cell contractility by fibronectin polymerization. J. Biol. Chem. 275, 10673-10682.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10673-10682
    • Hocking, D.C.1    Sottile, J.2    Langenbach, K.J.3
  • 28
    • 0032489680 scopus 로고    scopus 로고
    • 1-mediated signaling pathways by fibronectin's cell adhesion and matrix assembly domains
    • 1-mediated signaling pathways by fibronectin's cell adhesion and matrix assembly domains. J. Cell Biol. 141, 241-253.
    • (1998) J. Cell Biol. , vol.141 , pp. 241-253
    • Hocking, D.C.1    Sottile, J.2    McKeown-Longo, P.J.3
  • 29
    • 2142784516 scopus 로고    scopus 로고
    • MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover
    • Holmbeck, K. et al. (1999). MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover. Cell 99, 81-92.
    • (1999) Cell , vol.99 , pp. 81-92
    • Holmbeck, K.1
  • 30
    • 0004043397 scopus 로고
    • New York: Springer-Verlag
    • Hynes, R.O. (1990). Fibronectins. New York: Springer-Verlag.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 31
    • 0023025366 scopus 로고
    • Transforming growth factor-β stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix
    • Ignotz, R.A., and Massague, J. (1986). Transforming growth factor-β stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix. J. Biol. Chem. 261, 4337-4345.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4337-4345
    • Ignotz, R.A.1    Massague, J.2
  • 32
    • 0019230475 scopus 로고
    • Formation of cell-to-substrate contacts during fibroblast motility: An interference-reflexion study
    • Izzard, C.S., and Lochner, L.R. (1980). Formation of cell-to-substrate contacts during fibroblast motility: an interference-reflexion study. J. Cell Sci. 42, 81-116.
    • (1980) J. Cell Sci. , vol.42 , pp. 81-116
    • Izzard, C.S.1    Lochner, L.R.2
  • 33
    • 0034114114 scopus 로고    scopus 로고
    • Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions
    • Katz, B.Z., Zamir, E., Bershadsky, A., Kam, Z., Yamada, K.M., and Geiger, B. (2000). Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions. Mol. Biol. Cell 11, 1047-60.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1047-1060
    • Katz, B.Z.1    Zamir, E.2    Bershadsky, A.3    Kam, Z.4    Yamada, K.M.5    Geiger, B.6
  • 34
    • 0030582716 scopus 로고    scopus 로고
    • Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of cdk2 inhibitors
    • Koyama, H., Raines, E.W., Bornfeldt, K.E., Roberts, J.M., and Ross, R. (1996). Fibrillar collagen inhibits arterial smooth muscle proliferation through regulation of cdk2 inhibitors. Cell 87, 1069-1078.
    • (1996) Cell , vol.87 , pp. 1069-1078
    • Koyama, H.1    Raines, E.W.2    Bornfeldt, K.E.3    Roberts, J.M.4    Ross, R.5
  • 35
    • 0021782147 scopus 로고
    • The turnover and degradation of collagen
    • Krane, S.M. (1985). The turnover and degradation of collagen. Ciba Found. Symp. 114, 97-110.
    • (1985) Ciba Found. Symp. , vol.114 , pp. 97-110
    • Krane, S.M.1
  • 37
    • 0030860515 scopus 로고    scopus 로고
    • The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells
    • Lamaze, C., Fujimoto, L.M., Yin, H.L., and Schmid, S.L. (1997). The actin cytoskeleton is required for receptor-mediated endocytosis in mammalian cells. J. Biol. Chem. 272, 20332-20335.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20332-20335
    • Lamaze, C.1    Fujimoto, L.M.2    Yin, H.L.3    Schmid, S.L.4
  • 38
    • 0029002420 scopus 로고
    • A targeted mutation at the known collagenase cleavage site in mouse type I collagen impairs tissue remodeling
    • Liu, X., Wu, H., Byrne, M., Jeffrey, J., Krane, S., and Jaenisch, R. (1995). A targeted mutation at the known collagenase cleavage site in mouse type I collagen impairs tissue remodeling. J. Cell Biol. 130, 227-237.
    • (1995) J. Cell Biol. , vol.130 , pp. 227-237
    • Liu, X.1    Wu, H.2    Byrne, M.3    Jeffrey, J.4    Krane, S.5    Jaenisch, R.6
  • 39
    • 0030272712 scopus 로고    scopus 로고
    • Degradation of human plasma and extracellular matrix fibronectin by tissue type plasminogen activator and urokinase
    • Marchina, E., and Barlati, S. (1996). Degradation of human plasma and extracellular matrix fibronectin by tissue type plasminogen activator and urokinase. Int. J. Biochem. Cell Biol. 28, 1141-1150.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 1141-1150
    • Marchina, E.1    Barlati, S.2
  • 40
    • 0020072924 scopus 로고
    • Role of fibronectin in collagen deposition: Fab' to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix
    • McDonald, J.A., Kelley, D.G., and Broekelmann, T.J. (1982). Role of fibronectin in collagen deposition: Fab' to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix. J. Cell Biol. 92, 485-492.
    • (1982) J. Cell Biol. , vol.92 , pp. 485-492
    • McDonald, J.A.1    Kelley, D.G.2    Broekelmann, T.J.3
  • 41
    • 0021369175 scopus 로고
    • Binding and degradation of platelet thrombospondin by cultured fibroblasts
    • McKeown-Longo, P.J., Hanning, R., and Mosher, D.F. (1984). Binding and degradation of platelet thrombospondin by cultured fibroblasts. J. Cell Biol. 98, 22.
    • (1984) J. Cell Biol. , vol.98 , pp. 22
    • McKeown-Longo, P.J.1    Hanning, R.2    Mosher, D.F.3
  • 42
    • 0020601855 scopus 로고
    • Binding of plasma fibronectin to cell layers of human skin fibroblasts
    • McKeown-Longo, P.J., and Mosher, D.F. (1983). Binding of plasma fibronectin to cell layers of human skin fibroblasts. J. Cell Biol. 97, 466-472.
    • (1983) J. Cell Biol. , vol.97 , pp. 466-472
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 43
    • 0021926873 scopus 로고
    • Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts
    • McKeown-Longo, P.J., and Mosher, D.F. (1985). Interaction of the 70,000-mol-wt amino-terminal fragment of fibronectin with the matrix-assembly receptor of fibroblasts. J. Cell Biol. 100, 364-374.
    • (1985) J. Cell Biol. , vol.100 , pp. 364-374
    • McKeown-Longo, P.J.1    Mosher, D.F.2
  • 44
    • 0031886616 scopus 로고    scopus 로고
    • The αvβ5 integrin functions as an endocytic receptor for vitronectin
    • Memmo, L.M., and McKeown-Longo, P. (1998). The αvβ5 integrin functions as an endocytic receptor for vitronectin. J. Cell Sci. 111, 425-433.
    • (1998) J. Cell Sci. , vol.111 , pp. 425-433
    • Memmo, L.M.1    McKeown-Longo, P.2
  • 45
    • 0032559803 scopus 로고    scopus 로고
    • Inhibition of vascular smooth muscle cell growth by inhibition of fibronectin matrix assembly
    • Mercurius, K.W., and Morla, A.O. (1998). Inhibition of vascular smooth muscle cell growth by inhibition of fibronectin matrix assembly. Circ. Res. 82, 548-556.
    • (1998) Circ. Res. , vol.82 , pp. 548-556
    • Mercurius, K.W.1    Morla, A.O.2
  • 46
    • 0019941809 scopus 로고
    • Rapid methods for isolation of human plasma fibronectin
    • Miekka, S.I., Ingham, K.C., and Menache, D. (1982). Rapid methods for isolation of human plasma fibronectin. Thromb. Res. 27, 1-14.
    • (1982) Thromb. Res. , vol.27 , pp. 1-14
    • Miekka, S.I.1    Ingham, K.C.2    Menache, D.3
  • 48
    • 0028069348 scopus 로고
    • Superfibronectin is a functionally distinct form of fibronectin
    • Morla, A., Zhang, Z., and Ruoslahti, E. (1994). Superfibronectin is a functionally distinct form of fibronectin. Nature 367, 193-196.
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 49
    • 0020313151 scopus 로고
    • Synthesis and secretion of thrombospondin by cultured human endothelial cells
    • Mosher, D.F., Doyle, M.J., and Jaffe, E.A. (1982). Synthesis and secretion of thrombospondin by cultured human endothelial cells. J. Cell Biol. 93, 343.
    • (1982) J. Cell Biol. , vol.93 , pp. 343
    • Mosher, D.F.1    Doyle, M.J.2    Jaffe, E.A.3
  • 50
    • 0023432864 scopus 로고
    • Interactions of thrombospondin with endothelial cells: Receptor-mediated binding and degradation
    • Murphy-Ullrich, J.E., and Mosher, D.F. (1987). Interactions of thrombospondin with endothelial cells: receptor-mediated binding and degradation. J. Cell Biol. 105, 1603-1611.
    • (1987) J. Cell Biol. , vol.105 , pp. 1603-1611
    • Murphy-Ullrich, J.E.1    Mosher, D.F.2
  • 51
    • 0024245150 scopus 로고
    • Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo
    • O'Shea, K.S., and Dixit, V.M. (1988). Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo. J. Cell Biol. 107, 2737-2748.
    • (1988) J. Cell Biol. , vol.107 , pp. 2737-2748
    • O'Shea, K.S.1    Dixit, V.M.2
  • 52
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of α5β1 integrins promotes early fibronectin fibrillogenesis
    • Pankov, R., Cukierman, E., Katz, B.Z., Matsumoto, K., Lin, D.C., Lin, S., Hahn, C., and Yamada, K.M. (2000). Integrin dynamics and matrix assembly: tensin-dependent translocation of α5β1 integrins promotes early fibronectin fibrillogenesis. J. Cell Biol. 148, 1075-1090.
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5    Lin, S.6    Hahn, C.7    Yamada, K.M.8
  • 53
    • 0034693854 scopus 로고    scopus 로고
    • Focal adhesion kinase: A regulator of focal adhesion dynamics and cell movement
    • Parsons, J.T., Martin, K.H., Slack, J.K., Taylor, J.M., and Weed, S.A. (2000). Focal adhesion kinase: a regulator of focal adhesion dynamics and cell movement. Oncogene 19, 5606-5613.
    • (2000) Oncogene , vol.19 , pp. 5606-5613
    • Parsons, J.T.1    Martin, K.H.2    Slack, J.K.3    Taylor, J.M.4    Weed, S.A.5
  • 54
    • 0029907050 scopus 로고    scopus 로고
    • A polymeric form of fibronectin has antimetastatic effects against multiple tumor types
    • Pasqualini, R., Bourdoulous, S., Koivunen, E., Woods, V.L., and Ruoslahti, E. (1996). A polymeric form of fibronectin has antimetastatic effects against multiple tumor types. Nat. Med. 2, 1197-1203.
    • (1996) Nat. Med. , vol.2 , pp. 1197-1203
    • Pasqualini, R.1    Bourdoulous, S.2    Koivunen, E.3    Woods, V.L.4    Ruoslahti, E.5
  • 55
    • 0031252407 scopus 로고    scopus 로고
    • Targetting of the gene encoding fibrillin-1 recapitulates the vascular aspect of Marfan syndrome
    • Pereira, L. et al. (1997). Targetting of the gene encoding fibrillin-1 recapitulates the vascular aspect of Marfan syndrome. Nat. Genet. 17, 218-222.
    • (1997) Nat. Genet. , vol.17 , pp. 218-222
    • Pereira, L.1
  • 56
    • 0036473019 scopus 로고    scopus 로고
    • The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix
    • Pereira, M., Rybarczyk, B.J., Odrljin, T.M., Hocking, D.C., Sottile, J., and Simpson-Haidaris, P.J. (2002). The incorporation of fibrinogen into extracellular matrix is dependent on active assembly of a fibronectin matrix. J. Cell Sci. 115, 609-617.
    • (2002) J. Cell Sci. , vol.115 , pp. 609-617
    • Pereira, M.1    Rybarczyk, B.J.2    Odrljin, T.M.3    Hocking, D.C.4    Sottile, J.5    Simpson-Haidaris, P.J.6
  • 57
    • 0030614751 scopus 로고    scopus 로고
    • Ligation of integrin α5β1 is required for internalization of vitronectin by integrin αvβ3
    • Pijuan-Thompson, V., and Gladson, C.L. (1997). Ligation of integrin α5β1 is required for internalization of vitronectin by integrin αvβ3. J. Biol. Chem. 272, 2736-2743.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2736-2743
    • Pijuan-Thompson, V.1    Gladson, C.L.2
  • 58
    • 0024273065 scopus 로고
    • Fibronectin's amino-terminal matrix assembly site is located within the 29 kDa amino terminal domain containing five type 1 repeats
    • Quade, B.J., and McDonald, J.A. (1988). Fibronectin's amino-terminal matrix assembly site is located within the 29 kDa amino terminal domain containing five type 1 repeats. J. Biol. Chem. 263, 19602-19609.
    • (1988) J. Biol. Chem. , vol.263 , pp. 19602-19609
    • Quade, B.J.1    McDonald, J.A.2
  • 59
    • 0029608747 scopus 로고
    • Extracellular matrix incorporation of normal and NEM-alkylated fibronectin: Liver and spleen deposition
    • Rebres, R.A., McKeown-Longo, P.J., Vincent, P.A., Cho, E., and Saba, T.M. (1995). Extracellular matrix incorporation of normal and NEM-alkylated fibronectin: liver and spleen deposition. Am. J. Physiol. 269, G902-G912.
    • (1995) Am. J. Physiol. , vol.269
    • Rebres, R.A.1    McKeown-Longo, P.J.2    Vincent, P.A.3    Cho, E.4    Saba, T.M.5
  • 60
    • 0027598038 scopus 로고
    • Fibulin's organization into the extracellular matrix of fetal lung fibroblasts is dependent on fibronectin matrix assembly
    • Roman, J., and McDonald, J.A. (1993). Fibulin's organization into the extracellular matrix of fetal lung fibroblasts is dependent on fibronectin matrix assembly. Am. J. Respir. Cell Mol. Biol. 8, 538-545.
    • (1993) Am. J. Respir. Cell Mol. Biol. , vol.8 , pp. 538-545
    • Roman, J.1    McDonald, J.A.2
  • 61
    • 0037013254 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein mediates fibronectin catabolism and inhibits fibronectin accumulation on cell surfaces
    • Salicioni, A.M., Mizelle, K.S., Loukinova, E., Mikhailenko, I., Strickland, D.K., and Gonias, S.L. (2002). The low density lipoprotein receptor-related protein mediates fibronectin catabolism and inhibits fibronectin accumulation on cell surfaces. J. Biol. Chem. 277, 16160-16166.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16160-16166
    • Salicioni, A.M.1    Mizelle, K.S.2    Loukinova, E.3    Mikhailenko, I.4    Strickland, D.K.5    Gonias, S.L.6
  • 62
    • 0030447865 scopus 로고    scopus 로고
    • Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix
    • Sasaki, T., Wiedemann, H., Matzner, M., Chu, M.-L., and Timpl, R. (1996). Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix. J. Cell Sci. 109, 2895-2904.
    • (1996) J. Cell Sci. , vol.109 , pp. 2895-2904
    • Sasaki, T.1    Wiedemann, H.2    Matzner, M.3    Chu, M.-L.4    Timpl, R.5
  • 63
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro, S.D. (1998). Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr. Opin. Cell Biol. 10, 602-608.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 64
    • 0020062250 scopus 로고
    • Association of fibronectin and vinculin with focal contacts and stress fibers in stationary hamster fibroblasts
    • Singer, I.I. (1982). Association of fibronectin and vinculin with focal contacts and stress fibers in stationary hamster fibroblasts. J. Cell Biol. 92, 398-408.
    • (1982) J. Cell Biol. , vol.92 , pp. 398-408
    • Singer, I.I.1
  • 65
    • 0023680462 scopus 로고
    • Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation
    • Singer, I.I., Scott, S., Kawka, D.W., Kazazis, D.M., Gailit, J., and Ruoslhti, E. (1988). Cell surface distribution of fibronectin and vitronectin receptors depends on substrate composition and extracellular matrix accumulation. J. Cell Biol. 106, 2171-2182.
    • (1988) J. Cell Biol. , vol.106 , pp. 2171-2182
    • Singer, I.I.1    Scott, S.2    Kawka, D.W.3    Kazazis, D.M.4    Gailit, J.5    Ruoslhti, E.6
  • 66
    • 0027364276 scopus 로고
    • Protein kinase C modulation of fibronectin matrix assembly
    • Sommers, C.E., and Mosher, D.F. (1993). Protein kinase C modulation of fibronectin matrix assembly. J. Biol. Chem. 268, 22277-22280.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22277-22280
    • Sommers, C.E.1    Mosher, D.F.2
  • 67
    • 0034534561 scopus 로고    scopus 로고
    • Fibronectin polymerization stimulates cell growth by RGD-dependent and -independent mechanisms
    • Sottile, J., Hocking, D.C., and Langenbach, K.J. (2000). Fibronectin polymerization stimulates cell growth by RGD-dependent and -independent mechanisms. J. Cell Sci. 113, 4287-4299.
    • (2000) J. Cell Sci. , vol.113 , pp. 4287-4299
    • Sottile, J.1    Hocking, D.C.2    Langenbach, K.J.3
  • 68
    • 0031730895 scopus 로고    scopus 로고
    • Fibronectin matrix assembly enhances adhesion-dependent cell growth
    • Sottile, J., Hocking, D.C., and Swiatek, P. (1998). Fibronectin matrix assembly enhances adhesion-dependent cell growth. J. Cell Sci. 111, 2933-2943.
    • (1998) J. Cell Sci. , vol.111 , pp. 2933-2943
    • Sottile, J.1    Hocking, D.C.2    Swiatek, P.3
  • 70
    • 0028229056 scopus 로고
    • Assembly of amino-terminal fibronectin dimers into the extracellular matrix
    • Sottile, J., and Wiley, S. (1994). Assembly of amino-terminal fibronectin dimers into the extracellular matrix. J. Biol. Chem. 269, 17192-17198.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17192-17198
    • Sottile, J.1    Wiley, S.2
  • 71
    • 0002028777 scopus 로고    scopus 로고
    • Altered processing of fibronectin in mice lacking heparin. A role for heparin-dependent mast cell chymase in fibronectin degradation
    • Tchougounova, E., Forsberg, E., Angelborg, G., Kjellen, L., and Pejler, G. (2000). Altered processing of fibronectin in mice lacking heparin. A role for heparin-dependent mast cell chymase in fibronectin degradation. J. Biol. Chem. 16, 16.
    • (2000) J. Biol. Chem. , vol.16 , pp. 16
    • Tchougounova, E.1    Forsberg, E.2    Angelborg, G.3    Kjellen, L.4    Pejler, G.5
  • 73
    • 0027290714 scopus 로고
    • Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity
    • Tolsma, S.S., Volpert, O.V., Good, D.J., Frazier, W.A., Polverini, P.J., and Bouck, N. (1993). Peptides derived from two separate domains of the matrix protein thrombospondin-1 have anti-angiogenic activity. J. Cell Biol. 122, 497-511.
    • (1993) J. Cell Biol. , vol.122 , pp. 497-511
    • Tolsma, S.S.1    Volpert, O.V.2    Good, D.J.3    Frazier, W.A.4    Polverini, P.J.5    Bouck, N.6
  • 74
    • 0009482260 scopus 로고
    • Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H.T., Staehlin, T., and Grodon, J. (1979). Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.T.1    Staehlin, T.2    Grodon, J.3
  • 75
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signaling
    • Turner, C.E. (2000). Paxillin and focal adhesion signaling. Nat. Cell Biol. 2, E231-E236.
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 76
    • 0346963598 scopus 로고    scopus 로고
    • MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes
    • Vu, T.H., Shipley, J.M., Bergers, G., Berger, J.E., Helms, J.A., Hanahan, D., Shapiro, S.D., Senior, R.M., and Werb, Z. (1998). MMP-9/gelatinase B is a key regulator of growth plate angiogenesis and apoptosis of hypertrophic chondrocytes. Cell 93, 411-422.
    • (1998) Cell , vol.93 , pp. 411-422
    • Vu, T.H.1    Shipley, J.M.2    Bergers, G.3    Berger, J.E.4    Helms, J.A.5    Hanahan, D.6    Shapiro, S.D.7    Senior, R.M.8    Werb, Z.9
  • 78
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu, C., Keivens, V.M., O'Toole, T.E., McDonald, J.A., and Ginsberg, M.H. (1995). Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell 83, 715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 79
    • 0035802109 scopus 로고    scopus 로고
    • Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo
    • Xu, J., Rodriguez, D., Petitclerc, E., Kim, J.J., Hangai, M., Yuen, S.M., Davis, G.E., and Brooks, P.C. (2001). Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo. J. Cell Biol. 154, 1069-1079.
    • (2001) J. Cell Biol. , vol.154 , pp. 1069-1079
    • Xu, J.1    Rodriguez, D.2    Petitclerc, E.3    Kim, J.J.4    Hangai, M.5    Yuen, S.M.6    Davis, G.E.7    Brooks, P.C.8
  • 80
    • 0002490733 scopus 로고
    • Fibronectin domains and receptors
    • ed. D. F. Mosher, New York: Academic Press
    • Yamada, K. (1989). Fibronectin domains and receptors. In: Fibronectin, ed. D. F. Mosher, New York: Academic Press, 47-121.
    • (1989) Fibronectin , pp. 47-121
    • Yamada, K.1
  • 81
    • 0021242622 scopus 로고
    • Metabolism of proteoglycans in rat ovarian glanulosa cell culture. Multiple intracelluar degradative pathways and the effect of chloroquine
    • Yanagishita, M., and Hascall, V.C. (1984). Metabolism of proteoglycans in rat ovarian glanulosa cell culture. Multiple intracelluar degradative pathways and the effect of chloroquine. J. Biol. Chem. 259, 10270.
    • (1984) J. Biol. Chem. , vol.259 , pp. 10270
    • Yanagishita, M.1    Hascall, V.C.2
  • 82
    • 0028955748 scopus 로고
    • Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development
    • Yang, J.T., Rayburn, H., and Hynes, R.O. (1995). Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development. Development 121, 549-560.
    • (1995) Development , vol.121 , pp. 549-560
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 84
    • 0024059120 scopus 로고
    • Novel purification of vitronectin from human plasma by heparin affinity
    • Yatohgo, T., Izumi, M., Kashiwagi, H., and Hayashi, M. (1988). Novel purification of vitronectin from human plasma by heparin affinity. Cell Struct. Funct. 13, 281-292.
    • (1988) Cell Struct. Funct. , vol.13 , pp. 281-292
    • Yatohgo, T.1    Izumi, M.2    Kashiwagi, H.3    Hayashi, M.4
  • 85
    • 0031406090 scopus 로고    scopus 로고
    • The mast cell: Origin, morphology, distribution, and function
    • Yong, L.C. (1997). The mast cell: origin, morphology, distribution, and function. Exp. Toxicol. Pathol. 49, 409-424.
    • (1997) Exp. Toxicol. Pathol. , vol.49 , pp. 409-424
    • Yong, L.C.1
  • 86
    • 0033790713 scopus 로고    scopus 로고
    • Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts
    • Zamir, E. et al. (2000). Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts. Nat. Cell Biol. 2, 191-196.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 191-196
    • Zamir, E.1
  • 87
    • 0028004034 scopus 로고
    • Modulation of cell surface fibronectin assembly sites by lysophosphatidic acid
    • Zhang, Q., Checovich, W.J., Peters, D.M., Albrecht, R.M., and Mosher, D.F. (1994). Modulation of cell surface fibronectin assembly sites by lysophosphatidic acid. J. Cell Biol. 127, 1447-1459.
    • (1994) J. Cell Biol. , vol.127 , pp. 1447-1459
    • Zhang, Q.1    Checovich, W.J.2    Peters, D.M.3    Albrecht, R.M.4    Mosher, D.F.5
  • 88
    • 0033135378 scopus 로고    scopus 로고
    • Sphingosine 1-phosphate stimulates fibronectin matrix assembly through a Rho-dependent signal pathway
    • Zhang, Q., Peyruchaud, O., French, K.J., Magnusson, M.K., and Mosher, D.F. (1999). Sphingosine 1-phosphate stimulates fibronectin matrix assembly through a Rho-dependent signal pathway. Blood 93, 2984-2990.
    • (1999) Blood , vol.93 , pp. 2984-2990
    • Zhang, Q.1    Peyruchaud, O.2    French, K.J.3    Magnusson, M.K.4    Mosher, D.F.5
  • 89
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A.M., and Burridge, K. (1998). Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551.
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6


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